Ch. 3b Warm-Up What are the 4 classes of macromolecules? Give an example of each type of macromolecule.

Ch. 3b Warm-Up What are the 4 classes of macromolecules? Give an example of each. Draw and label the parts of an amino acid. How are 2 amino acids put together? Name the process and describe what happens. Draw a tripeptide. (Use Google for help) Label the peptide bonds.

Warm up Out of the following elements, which elements are present in carbohydrates,

Peptide Bonds

Ch. 3b Warm-Up Activity In your family groups, complete #1-5 on Activity 4/5.1: “How can you identify organic macromolecules?”

Ch. 3b Warm-Up What are the 4 levels of protein structure? What bonds are formed in each level? Which protein was involved in the curds & whey lab yesterday? Explain what happened to the milk to form the curds and whey.

Ch. 3b: The Structure and Function of Macromolecules

You Must Know The role of dehydration synthesis in the formation of organic compounds and hydrolysis in the digestion of organic compounds. How the sequence and subcomponents of the four groups of organic compounds determine their properties. The cellular functions of carbs, lipids, proteins, and nucleic acids. How changes in these organic molecules would affect their function.

You Must Know The 4 structural levels of proteins and how changes at any levels can affect the activity of the protein. How proteins reach their final shape (conformation), the denaturing impact that heat and pH can have on protein structure, and how these changes may affect the organism. Directionality influences structure and function of polymers, such as nucleic acids (5’ and 3’ ends) and proteins (amino and carboxyl ends).

ie. amino acid  peptide  polypeptide  protein Monomers Polymers Macromolecules Small organic Used for building blocks of polymers Connects with condensation reaction (dehydration synthesis) Long molecules of monomers With many identical or similar blocks linked by covalent bonds Giant molecules 2 or more polymers bonded together ie. amino acid  peptide  polypeptide  protein larger smaller

Dehydration Synthesis (Condensation Reaction) Hydrolysis Make polymers Breakdown polymers Monomers  Polymers Polymers  Monomers A + B  AB AB  A + B + H2O + + H2O +

Dehydration Synthesis

Hydrolysis

Proteomics: Analysis of proteins and sequences

I. Proteins “Proteios” = first or primary 50% dry weight of cells Contains: C, H, O, N, S Myoglobin protein

Protein Functions (+ examples) Enzymes (lactase) Defense (antibodies) Storage (milk protein = casein) Transport (hemoglobin) Hormones (insulin) Receptors Movement (motor proteins) Structure (keratin)

Overview of protein functions

Overview of protein functions

Four Levels of Protein Structure Primary Amino acid (AA) sequence 20 different AA’s peptide bonds link AA’s

Amino Acid “amino” : -NH2 “acid” : -COOH R group = side chains Properties: hydrophobic hydrophilic ionic (acids & bases) “amino” : -NH2 “acid” : -COOH

Four Levels of Protein Structure (continued) Secondary Gains 3-D shape (folds, coils) by H-bonding Alpha (α) helix, Beta (β) pleated sheet

Basic Principles of Protein Folding Hydrophobic AA buried in interior of protein (hydrophobic interactions) Hydrophilic AA exposed on surface of protein (hydrogen bonds) Acidic + Basic AA form salt bridges (ionic bonds). Cysteines can form disulfide bonds.

Four Levels of Protein Structure (continued) Tertiary Bonding between side chains (R groups) of amino acids H bonds, ionic bonds, disulfide bridges, hydrophobic interactions, van der Waals interactions

Four Levels of Protein Structure (continued) Quaternary 2+ polypeptides bond together

amino acids  polypeptides  protein Bonding (ionic & H) can create asymmetrical attractions

Chaperonins assist in proper folding of proteins

Protein structure and function are sensitive to chemical and physical conditions Unfolds or denatures if pH and temperature are not optimal

change in structure = change in function

X-ray crystallography used to determine the 3-D structure of proteins

Genomics: Analysis of genes and genomes

Function: store hereditary info II. Nucleic Acids Function: store hereditary info DNA RNA Double-stranded helix N-bases: A, G, C, Thymine Stores hereditary info Longer/larger Sugar: deoxyribose Single-stranded N-bases: A, G, C, Uracil Carry info from DNA to ribosomes tRNA, rRNA, mRNA, RNAi Sugar: ribose

Nucleotides: monomer of DNA/RNA Nucleotide = Sugar + Phosphate + Nitrogen Base

Nucleotide phosphate A – T Nitrogen G – C base 5-C sugar Purines Pyrimidines Adenine Guanine Cytosine Thymine (DNA) Uracil (RNA) Double ring Single ring 5-C sugar

Information flow in a cell: DNA  RNA  protein

Differ in position & orientation of glycosidic linkage III. Carbohydrates Fuel and building material Include simple sugars (fructose) and polymers (starch) Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O monosaccharide  disaccharide  polysaccharide Monosaccharides = monomers (eg. glucose, ribose) Polysaccharides: Storage (plants-starch, animals-glycogen) Structure (plant-cellulose, arthropod-chitin) Differ in position & orientation of glycosidic linkage

The structure and classification of some monosaccharides

Linear and ring forms of glucose

Carbohydrate synthesis

Cellulose vs. Starch Two Forms of Glucose:  glucose &  glucose

Cellulose vs. Starch Starch =  glucose monomers Cellulose =  glucose monomers

Storage polysaccharides of plants (starch) and animals (glycogen)

Structural polysaccharides: cellulose & chitin (exoskeleton)

IV. Lipids Fats (triglyceride): store energy Glycerol + 3 Fatty Acids saturated, unsaturated, polyunsaturated Steroids: cholesterol and hormones Phospholipids: lipid bilayer of cell membrane hydrophilic head, hydrophobic tails Hydrophilic head Hydrophobic tail

Have some C=C, result in kinks Saturated Unsaturated Polyunsaturated “saturated” with H Have some C=C, result in kinks In animals In plants Solid at room temp. Liquid at room temp. Eg. butter, lard Eg. corn oil, olive oil

Cholesterol, a steroid

The structure of a phospholipid

Hydrophobic/hydrophilic interactions make a phospholipid bilayer